LAPA_ASPOR
ID LAPA_ASPOR Reviewed; 377 AA.
AC Q2U1F3;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Leucine aminopeptidase A;
DE EC=3.4.11.-;
DE AltName: Full=Leucyl aminopeptidase A;
DE Short=LAPA;
DE Flags: Precursor;
GN Name=lapA; ORFNames=AO090011000052;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP PROTEIN SEQUENCE OF 80-86, INDUCTION, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=20803144; DOI=10.1007/s00284-010-9744-9;
RA Matsushita-Morita M., Tada S., Suzuki S., Hattori R., Marui J.,
RA Furukawa I., Yamagata Y., Amano H., Ishida H., Takeuchi M., Kashiwagi Y.,
RA Kusumoto K.;
RT "Overexpression and characterization of an extracellular leucine
RT aminopeptidase from Aspergillus oryzae.";
RL Curr. Microbiol. 62:557-564(2011).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19129648; DOI=10.1271/bbb.80500;
RA Liang Y., Pan L., Lin Y.;
RT "Analysis of extracellular proteins of Aspergillus oryzae grown on soy
RT sauce koji.";
RL Biosci. Biotechnol. Biochem. 73:192-195(2009).
CC -!- FUNCTION: Extracellular aminopeptidase that allows assimilation of
CC proteinaceous substrates. {ECO:0000269|PubMed:20803144}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Calcium, magnesium and manganese cations reduce
CC peptidase activity to 20.3-51.3 percent. The metal ion chelating
CC reagent EDTA almost completely inhibits activity. The protease
CC inhibitor bacitracin and the aminopeptidase B inhibitor bestatin, as
CC well as DTT and beta-mercaptoethanol act also as lap A inhibitorsD.
CC {ECO:0000269|PubMed:20803144}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.244 mM for Leu-p-nitroaniline {ECO:0000269|PubMed:20803144};
CC KM=0.782 mM for Phe-p-nitroaniline {ECO:0000269|PubMed:20803144};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:20803144};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:20803144};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19129648,
CC ECO:0000269|PubMed:20803144}.
CC -!- INDUCTION: Expressed at higher level at alkaline conditions. May be
CC under the control of pacC, the transcription factor that regulates pH-
CC conditional gene expression. Expression is very low under normal
CC condition, salt condition and heat-stress condition.
CC {ECO:0000269|PubMed:20803144}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC {ECO:0000305}.
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DR EMBL; AP007171; BAE64612.1; -; Genomic_DNA.
DR RefSeq; XP_001825745.1; XM_001825693.1.
DR PDB; 6ZEP; X-ray; 1.61 A; A=1-377.
DR PDB; 6ZEQ; X-ray; 1.97 A; A=1-377.
DR PDB; 7OEZ; X-ray; 2.48 A; A=77-377.
DR PDBsum; 6ZEP; -.
DR PDBsum; 6ZEQ; -.
DR PDBsum; 7OEZ; -.
DR AlphaFoldDB; Q2U1F3; -.
DR SMR; Q2U1F3; -.
DR STRING; 510516.Q2U1F3; -.
DR MEROPS; M28.022; -.
DR EnsemblFungi; BAE64612; BAE64612; AO090011000052.
DR GeneID; 5997848; -.
DR KEGG; aor:AO090011000052; -.
DR VEuPathDB; FungiDB:AO090011000052; -.
DR HOGENOM; CLU_025866_0_0_1; -.
DR OMA; IQFDMTG; -.
DR Proteomes; UP000006564; Chromosome 7.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IDA:AspGD.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Metal-binding; Protease; Reference proteome;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..79
FT /evidence="ECO:0000269|PubMed:20803144"
FT /id="PRO_0000412395"
FT CHAIN 80..377
FT /note="Leucine aminopeptidase A"
FT /id="PRO_0000412396"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..314
FT /evidence="ECO:0000250"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 120..140
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:6ZEP"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:6ZEP"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 221..231
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 317..322
FT /evidence="ECO:0007829|PDB:6ZEP"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:6ZEQ"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:6ZEP"
FT HELIX 354..372
FT /evidence="ECO:0007829|PDB:6ZEP"
SQ SEQUENCE 377 AA; 41105 MW; FC46EBEF3195CA76 CRC64;
MRFLPCIATL AATASALAIG DHVRSDDQYV LELAPGQTKV VTEAEKWALR AEGKRFFDIT
ERASSLELAS NKKQKLAVTY PDSVQHNETV QNLIKSLDKK NFETVLQPFS EFHNRYYKSD
NGKKSSEWLQ GKIQEIISAS GAKGVTVEPF KHSFPQSSLI AKIPGKSDKT IVLGAHQDSI
NLDSPSEGRA PGADDDGSGV VTILEAFRVL LTDEKVAAGE APNTVEFHFY AGEEGGLLGS
QDIFEQYSQK SRDVKAMLQQ DMTGYTKGTT DAGKPESIGI ITDNVDENLT KFLKVIVDAY
CTIPTVDSKC GYGCSDHASA TKYGYPAAFA FESAFGDDSP YIHSADDTIE TVNFDHVLQH
GRLTLGFAYE LAFADSL
